6GZS

Structure of Chlamydia trachomatis effector protein ChlaDUB1 bound to ubiquitin

6GZS の概要

• エントリーDOI: 10.2210/pdb6gzs/pdb
• 分子名称: Deubiquitinase and deneddylase Dub1, Polyubiquitin-B, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: enzyme, ce clan, deubiquitinase, acetyltransferase, hydrolase
• 由来する生物種: Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40072.27

構造登録者

Pruneda, J.N.,Komander, D. (登録日: 2018-07-05, 公開日: 2018-11-14, 最終更新日: 2025-04-09)

主引用文献

Pruneda, J.N.,Bastidas, R.J.,Bertsoulaki, E.,Swatek, K.N.,Santhanam, B.,Clague, M.J.,Valdivia, R.H.,Urbe, S.,Komander, D.
A Chlamydia effector combining deubiquitination and acetylation activities induces Golgi fragmentation.
Nat Microbiol, 3:1377-1384, 2018

PubMed Abstract: Pathogenic bacteria are armed with potent effector proteins that subvert host signalling processes during infection. The activities of bacterial effectors and their associated roles within the host cell are often poorly understood, particularly for Chlamydia trachomatis, a World Health Organization designated neglected disease pathogen. We identify and explain remarkable dual Lys63-deubiquitinase (DUB) and Lys-acetyltransferase activities in the Chlamydia effector ChlaDUB1. Crystal structures capturing intermediate stages of each reaction reveal how the same catalytic centre of ChlaDUB1 can facilitate such distinct processes, and enable the generation of mutations that uncouple the two activities. Targeted Chlamydia mutant strains allow us to link the DUB activity of ChlaDUB1 and the related, dedicated DUB ChlaDUB2 to fragmentation of the host Golgi apparatus, a key process in Chlamydia infection for which effectors have remained elusive. Our work illustrates the incredible versatility of bacterial effector proteins, and provides important insights towards understanding Chlamydia pathogenesis.

PubMed: 30397340
DOI: 10.1038/s41564-018-0271-y

実験手法

X-RAY DIFFRACTION (1.9 Å)